Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.

@article{Pratt2003RegulationOS,
  title={Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.},
  author={William Brewster Pratt and David Orville Toft},
  journal={Experimental biology and medicine},
  year={2003},
  volume={228 2},
  pages={
          111-33
        }
}
Nearly 100 proteins are known to be regulated by hsp90. Most of these substrates or "client proteins" are involved in signal transduction, and they are brought into complex with hsp90 by a multiprotein hsp90/hsp70-based chaperone machinery. In addition to binding substrate proteins at the chaperone site(s), hsp90 binds cofactors at other sites that are part of the heterocomplex assembly machinery as well as immunophilins that connect assembled substrate*hsp90 complexes to protein-trafficking… CONTINUE READING

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